Journal
PLANT JOURNAL
Volume 37, Issue 5, Pages 678-693Publisher
WILEY
DOI: 10.1111/j.1365-313X.2003.01995.x
Keywords
mu-adaptin; vacuolar transport; tyrosine-based sorting motif
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In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) mu-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXO). We have analyzed the function of the muA-adaptin, one of the five mu-adaptins from Arabidopsis thaliana, by pull-down assays and plasmon resonance measurements using its receptor-binding domain (RBD) fused to a histidine tag. We show that this adaptin is able to bind the consensus tyrosine motif YXXO from the pea vacuolar sorting receptor (VSR)-PS1, as well as from the mammalian trans-Golgi network (TGN)38 protein. Moreover, the tyrosine residue was revealed to be crucial for binding of the complete cytoplasmic tail of VSR-PS1 to the plant muA-adaptin. The trans-Golgi localization of the muA-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.
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